Skip to main content
SpringerLink
Log in

Effect of tungstate on pea root growth and protein tyrosine phosphorylation

  • Research Papers
  • Published:
Russian Journal of Plant Physiology Aims and scope Submit manuscript

Abstract

Tungsten belong to heavy metal group, which physiological, biochemical, and molecular action mechanisms are essentially unstudied despite metal wide application in light, heavy, and military industries and the gradual accumulation in the environment. Protein phosphorylation/dephosphorylation (one of the most important posttranslational modifications) is a highly conserved mechanism of intracellular signaling and regulation of many processes of cell activity. Protein tyrosine phosphorylation/dephosphorylation is required for the cell cycle processing, plant growth and differentiation. In this work, the effects of sodium tungstate on pea (Pisum sativum L. cv. Truzhenik) root growth, protein tyrosine phosphorylation, and phosphatase activity in the roots were studied. It was shown that sodium tungstate suppressed growth, changed the mitotic index in the root meristem, and delayed cells at some mitosis phases. Under the influence of tungstate, hydrogen peroxide accumulated in the roots and phosphatase activity was inhibited. It was established by two-dimension electrophoresis and immunoblotting with the highly specific to phosphotyrosine antibody (PY20) that tungstate treatment increased both the number of such proteins and their specific phosphorylation. It is supposed that the inhibition of protein tyrosine phosphatases was one of the reasons for tungstateinduced pea root growth inhibition.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

Abbreviations

2DE:

two-dimensional electrophoresis

HM:

heavy metals

MI:

mitotic index

PK:

protein kinase

PMSF:

phenylmethylsulfonyl fluoride

pNPP:

p-nitrophenyl phosphate

PP:

protein phosphatase

PTM:

posttranslational modification

PTK:

protein tyrosine kinase

PTP:

protein tyrosine phosphatase

STP:

specific tyrosine phosphorylation.

References

  1. L’vov, N.P., Nosikov, A.N., and Antipov, A.N., Tungsten-containing enzymes, Biochemistry (Moscow), 2002, vol. 67, pp. 196–200.

    Article  Google Scholar 

  2. Toxicological Profile for Tungsten. Agency for toxic substances and disease registry (ATSDR). Atlanta (GA): U.S. Dept. Health and Human Services, Public Health Service, 2005.

  3. Van der Voet, G., Todorov, T.I., Centeno, J.A., Jonas, W., Ives, J., and Mullick, F.G., Metals and health: a clinical toxicological perspective on tungsten and revive of the literature, Milit. Med., 2007, vol. 172, pp. 1002–1005.

    Google Scholar 

  4. Thomas, V.G., Roberts, M.J., and Harrison, P.T.C., Assessment of the environmental toxicity and carcinogenicity of tungsten-based shot, Ecotoxicol. Environ. Safety, 2009, vol. 72, pp. 1031–1037.

    Article  PubMed  CAS  Google Scholar 

  5. Johnson, D.R., Inouye, L.S., Bednar, A.J., Clarke, J.U., Winfield, L.E., Boyd, R.E., Ang, C.Y., and Goss, J., Tungsten bioavailability and toxicity in sunflowers (Hellianthus annuus L.), Land Cont. Reclam., 2009, vol. 17, pp. 141–151.

    Article  Google Scholar 

  6. Adamakis, I.-D.S., Panteris, E., and Eleftheriou, E.P., The fatal effect of tungsten on Pisum sativum L. root cells: indications for endoplasmic reticulum stressinduced programmed cell death, Planta, 2011, vol. 234, pp. 21–34.

    Article  PubMed  CAS  Google Scholar 

  7. Adamakis, I.-D.S., Panteris, E., and Eleftheriou, E.P., Tungsten affects the cortical microtubules of Pisum sativum root cells: experiments on tungsten-molybdenum antagonism, Plant Biol., 2010, vol. 123, pp. 114–124.

    Article  Google Scholar 

  8. De la Fuente van Bentem, S. and Hirt, H., Protein tyrosine phosphorylation in plants: more abundant than expected? Trends Plant Sci., 2009, vol. 14, pp. 71–76.

    Article  PubMed  Google Scholar 

  9. Karimova, F.G., Protein tyrosine phosphorylation, Kletochnaya signalizatsiya (Signaling in the Cell), Grechkin, A.N., Ed., Kazan: Fen, 2010, pp. 37–45.

    Google Scholar 

  10. Zhang, K.D., Letham, D., and John, P., Cytokinin control the cell cycle at mitosis by stimulating the tyrosine dephosphorylation and activation of p34cdk2-like H1 histone kinase, Planta, 1996, vol. 200, pp. 2–12.

    Article  PubMed  CAS  Google Scholar 

  11. Petrova, N.V. and Karimova, F.G., effects of redox agents on protein tyrosine phosphorylation in pea roots, Russ. J. Plant Physiol., 2011, vol. 58, pp. 906–913.

    Article  Google Scholar 

  12. Krutetskaya, Z.B., Lebedev, O.E., and Kurilova, L.S., Mekhanizmy vnutrikletochnoi signalizatsii (Mechanisms for Intracellular Signaling), St. Petersburg: St. Petersburg Gos. Univ., 2003.

    Google Scholar 

  13. Wolff, S.P., Ferrous ion oxidation in presence of ferric ion indicator xylenol orange for measurement of hydroperoxides, Methods Enzymol., 1994, vol. 223, pp. 182–189.

    Article  Google Scholar 

  14. Seregin, I.V. and Ivanov, V.B., Physiological aspects of cadmium and lead toxic effects on higher plants, Russ. J. Plant Physiol., 2001, vol. 48, pp. 523–544.

    Article  CAS  Google Scholar 

  15. Wierzbicka, M., Resumption of mitotic activity in Allium cepa root tips during treatment with lead salts, Environ. Exp. Bot., 1994, vol. 34, pp. 173–180.

    Article  CAS  Google Scholar 

  16. Dovgalyuk, A.I., Kalinyak, T.B., and Blyum, Ya.B., Use of Allium cepa root apical meristem for heavy metal and Al phyto- and cytotoxic activity evaluation, Tsitol. Genet., 2001, vol. 35, pp. 3–9.

    Google Scholar 

  17. Mukhitov, A.R., Effect of colchicine on the genetic stability and morphogenic activity of Fagopyrum tataricum (L.) Gaertn calli, Cand. Sci. (Biol.) Dissertation, Kazan: Kazan Gos. Univ., 2000.

    Google Scholar 

  18. Alex, S. and Dupuis, P., FT-IR and Raman investigation of cadmium binding by DNA, Inorg. Chim. Acta, 1989, vol. 157, pp. 271–281.

    Article  CAS  Google Scholar 

  19. Schutzendubel, A. and Polle, A., Plant responses to abiotic stresses: heavy metal-induced oxidative stress and protection by mycorrhization, J. Exp. Bot., 2002, vol. 372, pp. 1351–1365.

    Article  Google Scholar 

  20. Johanes, R., Redox regulation of the Cdc25 phosphatases, Antiox. Redox Signal., 2005, vol. 7, pp. 761–768.

    Article  Google Scholar 

  21. Kreslavski, V.D., Los, D.A., Allakhverdiev, S.I., and Kuznetsov, Vl.V., Signaling role of reactive oxygen species in plants under stress, Russ. J. Plant Physiol., 2012, vol. 59, pp. 141–154.

    Article  CAS  Google Scholar 

  22. Vranova, E., Inze, D., and van Breusegem, F., Signal transduction during oxidative stress, J. Exp. Bot., 2002, vol. 53, pp. 1227–1236.

    Article  PubMed  CAS  Google Scholar 

  23. Chiarugi, P. and Buricchi, F., Protein tyrosine phosphorylation and reversible oxidation: two cross-talking posttranslation modifications, Antiox. Redox Signal., 2007, vol. 9, pp. 1–24.

    Article  CAS  Google Scholar 

  24. Karimova, F.G. and Gazizova, N.I., Tungsten-induced protein tyrosine phosphorylation in Pisum sativum L. roots, Mater. 1 Mezhd. internet-konf. “Rasteniya i mikroorganizmy” (Proc. 1st Int. Internet-Conf. “Plants and Microorganisms”), Kazan, 2011, pp. 126–128.

    Google Scholar 

  25. Guo, Y.-L. and Roux, S.J., Partial purification and characterization of an enzyme from pea nuclei with protein tyrosine phosphatase activity, Plant Physiol., 1995, vol. 107, pp. 167–175.

    PubMed  CAS  Google Scholar 

  26. Reynolds, R.A., Yem, A.W., Wolfe, C.L., Deibel, M.R., Jr., Chidester, C.G., and Watenpaugh, K.D., Crystal structure of the catalytic subunit of Cdc25B required for G2/M phase transition of cell cycle, J. Mol. Biol., 1999, vol. 293, pp. 559–568.

    Article  PubMed  CAS  Google Scholar 

  27. Wang, Z., Kar, S., and Carr, B.I., Cdc25 protein phosphatase: a therapeutic target for liver cancer therapies, Anti-Canc. Ag. Med. Chem., 2008, vol. 8, pp. 863–871.

    Article  CAS  Google Scholar 

  28. Haque, S.J., Flati, V., Deb, A., and Wiliams, B.R.G., Roles of protein-tyrosine phosphatases in stat-1-mediated cell signaling, J. Biol. Chem., 1995, vol. 270, pp. 25709–25714.

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Kazan Institute of Biochemistry and Biophysics, Kazan Research Center, Russian Academy of Sciences, ul. Lobachevskogo 2/31, Kazan, Tatarstan, 420111, Russia

    N. I. Gazizova, N. V. Petrova & F. G. Karimova

Authors
  1. N. I. Gazizova
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. N. V. Petrova
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. F. G. Karimova
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to N. I. Gazizova.

Additional information

Original Russian Text © N.I. Gazizova, N.V. Petrova, F.G. Karimova, 2013, published in Fiziologiya Rastenii, 2013, Vol. 60, No. 6, pp. 819–827.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Gazizova, N.I., Petrova, N.V. & Karimova, F.G. Effect of tungstate on pea root growth and protein tyrosine phosphorylation. Russ J Plant Physiol 60, 776–784 (2013). https://doi.org/10.1134/S1021443713050051

Download citation

  • Received:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1134/S1021443713050051

Keywords

Search

Navigation